Canine GDP-ran R76E mutant. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 Jun 1999.
Explore 1QG2 in 3D Show helices and sheets RCSB PDB PDBe
1QG2 contains 13 α-helices and 12 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-16 | 7 | 1 |
| α-helix | 23-28 | 6 | |
| β-strand | 30 | 1 | 2 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 1 |
| β-strand | 45-54 | 10 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 69-72 | 4 | |
| α-helix | 74-76 | 3 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 133-135 | 3 | |
| β-strand | 145-148 | 4 | 1 |
| β-strand | 150 | 1 | 3 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 3 |
| α-helix | 158-169 | 12 | |
| β-strand | 176-178 | 3 | 1 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 2 |
| α-helix | 183-185 | 3 | |
| α-helix | 191-205 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (RAN) | A | protein | 216 | Canis lupus familiaris | P62825 (AlphaFold model) |
>1QG2_1 PROTEIN (RAN) (chains A) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLEDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Engineered mutants in the switch II loop of Ran define the contribution made by key residues to the interaction with nuclear transport factor 2 (NTF2) and the role of this interaction in nuclear protein import. Kent, H.M., Moore, M.S., Quimby, B.B. et al. J Mol Biol (1999) 289:565-577. DOI 10.1006/jmbi.1999.2775 · PubMed
Other PDB entries of the same protein (UniProt P62825 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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